High impact information on BCK1

• Expression of the MEKK catalytic domain, but not the full-length molecule, corrected the cell-lysis defect of a pkc1 delta mutant that lacks a protein kinase C homolog that functions upstream of Bck1p [1].
• Overexpression of MLP1 suppresses the caffeine-sensitive phenotype of the bck1 delta mutation [2].
• The putative catalytic domain of Mkh1 is 54% identical to the catalytic domain of S. cerevisiae Bck1, the most closely related protein [3].
• To search for genes that interact with the SLK1-SLT2 pathway, a synthetic lethal suppression screen was carried out [4].
• Slk1p has an important role in morphogenesis and growth control, and deletions of the SLK1 gene are lethal in a spa2-delta mutant background [4].

Biological context of BCK1

• Sequence and function analysis of a 9.74 kb fragment of Saccharomyces cerevisiae chromosome X including the BCK1 gene [5].
• High sequence similarity was detected to members of the mitogen-activated serine/threonine protein (MAP) kinase family involved in signal transduction: STE20, STE11, BCK1, Byr2 and p65PAK [6].
• The BCK1 gene possesses a 4.4-kb uninterrupted open reading frame predicted to encode a 163-kDa protein kinase [7].
• Suppressor alleles of BCK1 differed from the wild-type gene in a region surrounding a potential PKC phosphorylation site immediately upstream of the predicted catalytic domain [7].
• All of the suppressor mutations were dominant for suppressor function and defined a single locus, which was designated BCK1 (for bypass of C kinase) [7].

Anatomical context of BCK1

• The upstream mitogen-activated protein kinase kinase kinase (MAPKKK, or MEKK), BCK1, is an essential component in this pathway for maintaining cell-wall integrity and preventing fungal cell lysis [8].

Associations of BCK1 with chemical compounds

• The putative SSP31 protein also has a hybrid structure of serine/threonine and tyrosine kinases in the diagnostic subdomains for target specificity of protein kinases [9].

Regulatory relationships of BCK1

• Pkc1 has been proposed to regulate a protein kinase cascade which includes the Bck1, Mkk1/Mkk2 and Mpk1 kinases [10].
• The SSP31 gene of S. cerevisiae was isolated as a chromosomal DNA fragment suppressing the thermosensitive cell growth of the smp3 mutant when it was ligated into the low-copy vector, YCp50 [9].

Other interactions of BCK1

• The MPK1 gene was isolated as a dosage-dependent suppressor of the cell lysis defect associated with deletion of the BCK1 gene [11].
• This phenotypic defect is similar to that associated with deletion of the BCK1 gene, which is thought to function in the pathway mediated by PCK1 [12].
• The different slk1 mutant defects are partially rescued by an extra copy of the SSD1/SRK1 gene [13].
• The BCK1 gene product is not closely related to any known protein kinase, sharing only 45% amino acid identity with its closest known relative (the STE11-encoded protein kinase) through a region restricted to its putative C-terminal catalytic domain [7].
• A new protein kinase, SSP31, modulating the SMP3 gene-product involved in plasmid maintenance in Saccharomyces cerevisiae [9].

Analytical, diagnostic and therapeutic context of BCK1

• The SLK1 gene has been cloned, and sequence analysis predicts that the SLK1 protein is 1,478 amino acid residues in length [13].

References